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Volumn 31, Issue 9, 1999, Pages 961-975

Fumarate metabolism and the microaerophily of Campylobacter species

Author keywords

Campylobacter; Fumarate metabolism; Fumarate reductase; Inhibitors microaerophily

Indexed keywords

ANTHELMINTIC AGENT; DRUG DERIVATIVE; FUMARIC ACID DERIVATIVE; LEVAMISOLE; MALIC ACID; MALIC ACID DERIVATIVE; MORANTEL; OXANTEL; PYRANTEL; TIABENDAZOLE;

EID: 0033192048     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00062-X     Document Type: Article
Times cited : (31)

References (54)
  • 2
    • 0028469426 scopus 로고
    • Specific in situ hybridization of the intracellular organism of porcine proliferative enteropathy
    • C.J. Gebhart, S. McOrist, G.H. Lawson, J.E. Collins, G.E. Ward, Specific in situ hybridization of the intracellular organism of porcine proliferative enteropathy, Vet. Pathol. 31 (1994) 462-467.
    • (1994) Vet. Pathol. , vol.31 , pp. 462-467
    • Gebhart, C.J.1    McOrist, S.2    Lawson, G.H.3    Collins, J.E.4    Ward, G.E.5
  • 4
    • 0027455201 scopus 로고
    • Septic abortion associated with Campylobacter fetus subspecies fetus infection: Case report and review of literature
    • R.W. Sauerwein, J. Bisseling, A.M. Horrevorts, Septic abortion associated with Campylobacter fetus subspecies fetus infection: case report and review of literature, Infection 21 (1993) 331-333.
    • (1993) Infection , vol.21 , pp. 331-333
    • Sauerwein, R.W.1    Bisseling, J.2    Horrevorts, A.M.3
  • 5
    • 0028456273 scopus 로고
    • Evaluation of cultural methods and selective media for the isolation of Campylobacter fetus subsp. venerealis from cattle
    • S. Hum, J. Brunner, A. Mclnnes, G. Mendoza, J. Stephens, Evaluation of cultural methods and selective media for the isolation of Campylobacter fetus subsp. venerealis from cattle, Aust. Vet. J. 71 (1994) 184-186.
    • (1994) Aust. Vet. J. , vol.71 , pp. 184-186
    • Hum, S.1    Brunner, J.2    Mclnnes, A.3    Mendoza, G.4    Stephens, J.5
  • 6
    • 0022500475 scopus 로고
    • Microaerophiliy and oxygen toxicity
    • N.R. Krieg, P.S. Huffman, Microaerophiliy and oxygen toxicity, Ann. Rev. Microbiol. 40 (1986) 107-130.
    • (1986) Ann. Rev. Microbiol. , vol.40 , pp. 107-130
    • Krieg, N.R.1    Huffman, P.S.2
  • 7
    • 0020433098 scopus 로고
    • Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen
    • G.M. Carlone, J. Lascelles, Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen, J. Bacteriol. 152 (1982) 306-314.
    • (1982) J. Bacteriol. , vol.152 , pp. 306-314
    • Carlone, G.M.1    Lascelles, J.2
  • 8
    • 0022392612 scopus 로고
    • Participation of cytochromes in some oxidation-reduction systems in Campylobacter fetus
    • J. Lascelles, K.M. Calder, Participation of cytochromes in some oxidation-reduction systems in Campylobacter fetus, J. Bacteriol. 164 (1985) 401-409.
    • (1985) J. Bacteriol. , vol.164 , pp. 401-409
    • Lascelles, J.1    Calder, K.M.2
  • 9
    • 0029931613 scopus 로고    scopus 로고
    • The respiratory chain of Helicobacter pylori: Identification of cytochromes and the effects of oxygen on cytochrome and menaquinone levels
    • S.W. Marcelli, H.T. Chang, T. Chapman, P.A. Chalk, R.J. Miles, R.K. Poole, The respiratory chain of Helicobacter pylori: identification of cytochromes and the effects of oxygen on cytochrome and menaquinone levels, FEMS Microbiol. Lett. 138 (1996) 59-64.
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 59-64
    • Marcelli, S.W.1    Chang, H.T.2    Chapman, T.3    Chalk, P.A.4    Miles, R.J.5    Poole, R.K.6
  • 10
    • 0029934464 scopus 로고    scopus 로고
    • Ce-type cytochrome c oxidase terminates the respiratory chain in Helicobacter pylori
    • K. Nagata, S. Tsukita, T. Tamura, N. Sone, ce-type cytochrome c oxidase terminates the respiratory chain in Helicobacter pylori, Microbioloy 142 (1996) 1757-1763.
    • (1996) Microbioloy , vol.142 , pp. 1757-1763
    • Nagata, K.1    Tsukita, S.2    Tamura, T.3    Sone, N.4
  • 11
    • 0017832453 scopus 로고
    • The genus Campylobacter
    • R.M. Smibert, The genus Campylobacter, Ann. Rev. Microbiol. 32 (1978) 673-709.
    • (1978) Ann. Rev. Microbiol. , vol.32 , pp. 673-709
    • Smibert, R.M.1
  • 12
    • 0008432592 scopus 로고    scopus 로고
    • Utilization of amino acids by Campylobacter jejuni
    • D.G. Newell, J.M. Ketley, R.A. Feldman (Eds.), Plenum Press, New York
    • G.L. Mendz, S.L. Hazell, Utilization of amino acids by Campylobacter jejuni, in: D.G. Newell, J.M. Ketley, R.A. Feldman (Eds.), Campylobacters Helicobacters and Related Organisms, Plenum Press, New York, 1996, pp. 67-73.
    • (1996) Campylobacters Helicobacters and Related Organisms , pp. 67-73
    • Mendz, G.L.1    Hazell, S.L.2
  • 13
    • 0000203392 scopus 로고
    • Chemotherapy of gasteointestinal helminths
    • H. Vanden Bossche, D. Thienpont, T.G. Jansssens (Eds.), Springer-Verlag, Berlin
    • H. Vanden Bossche, Chemotherapy of gasteointestinal helminths, in: H. Vanden Bossche, D. Thienpont, T.G. Jansssens (Eds.), Handbook of Experimental Pharmacology, 77, Springer-Verlag, Berlin, 1985, pp. 125-181.
    • (1985) Handbook of Experimental Pharmacology , vol.77 , pp. 125-181
    • Vanden Bossche, H.1
  • 15
    • 0014757386 scopus 로고
    • General method applicable to the search for similarities in the amino acid sequence of two proteins
    • S.B. Needleman, C.D. Wunsch, General method applicable to the search for similarities in the amino acid sequence of two proteins, J. Mol. Biol. 48 (1970) 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 16
    • 0028856397 scopus 로고
    • Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumA genes of Escherichia coll: Role of the arcA, fnr, and soxK. gene products
    • S.J. Park, R.P. Gunsalus, Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumA genes of Escherichia coll: role of the arcA, fnr, and soxK. gene products, J. Bacteriol. 177 (1995) 6255-6262.
    • (1995) J. Bacteriol. , vol.177 , pp. 6255-6262
    • Park, S.J.1    Gunsalus, R.P.2
  • 17
    • 0002961439 scopus 로고    scopus 로고
    • Tricarboxylic acid cycle and glyoxlate bypass
    • F.C. Neidhard, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), ASM Press, Washington, DC, Second edition
    • J.E. Cronan Jr, D. LaPorte, Tricarboxylic acid cycle and glyoxlate bypass, in: F.C. Neidhard, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), Eschericia coll and Salmonella - Cellular and Molecular Biology, 1, ASM Press, Washington, DC, 1996, pp. 206-216 Second edition.
    • (1996) Eschericia Coll and Salmonella - Cellular and Molecular Biology , vol.1 , pp. 206-216
    • Cronan Jr., J.E.1    LaPorte, D.2
  • 18
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • F.C. Neidhard III, R. Curtiss, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), ASM Press, Washington, DC, Second edition.
    • R.B. Gennis, V. Stewart, Respiration, in: F.C. Neidhard III, R. Curtiss, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), Eschericia coll and Salmonella: Cellular and Molecular Biology, 1, ASM Press, Washington, DC, 1996, pp. 217-261 Second edition.
    • (1996) Eschericia Coll and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 19
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • F.C. Neidhard, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), ASM Press, Washington, DC, Second edition
    • J.E. Cronan Jr, C.O. Rock, Biosynthesis of membrane lipids, in: F.C. Neidhard, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Eds.), Eschericia coll and Salmonella -Cellular and Molecular Biology, 1, ASM Press, Washington, DC, 1996, pp. 612-636 Second edition.
    • (1996) Eschericia Coll and Salmonella -Cellular and Molecular Biology , vol.1 , pp. 612-636
    • Cronan Jr., J.E.1    Rock, C.O.2
  • 20
    • 0025113604 scopus 로고
    • The fumarate reductase operon of Wollnella succlnogenes: Sequence and expression of the frdA and frdB genes
    • F. Lauterbach, C. Kortner, S.P.J. Albracht, G. Unden, A. Kroger, The fumarate reductase operon of Wollnella succlnogenes: sequence and expression of the frdA and frdB genes, Arch. Microbiol. 154 (1990) 386-393.
    • (1990) Arch. Microbiol. , vol.154 , pp. 386-393
    • Lauterbach, F.1    Kortner, C.2    Albracht, S.P.J.3    Unden, G.4    Kroger, A.5
  • 22
    • 0031811217 scopus 로고    scopus 로고
    • Two membrane anchors of Wollnella succlnogenes hydrogenase and their function in fumarate and polysulfide respiration
    • R. Gross, J. Simon, F. Theis, A. Kröger, Two membrane anchors of Wollnella succlnogenes hydrogenase and their function in fumarate and polysulfide respiration, Arch. Microbiol. 170 (1998) 50-58.
    • (1998) Arch. Microbiol. , vol.170 , pp. 50-58
    • Gross, R.1    Simon, J.2    Theis, F.3    Kröger, A.4
  • 23
    • 0030967062 scopus 로고    scopus 로고
    • Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes
    • R. Lenger, U. Herrmann, R. Gross, J. Simon, A. Kroger, Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes, Eur. J. Biochem. 246 (1997) 646-651.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 646-651
    • Lenger, R.1    Herrmann, U.2    Gross, R.3    Simon, J.4    Kroger, A.5
  • 24
    • 0025912548 scopus 로고
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
    • M. Bokranz, M. Gutmann, C. Kortner, E. Kojro, F. Fahrenholz, F. Lauterbach, A. Kroger, Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes, Arch. Microbiol. 156 (1991) 119-128.
    • (1991) Arch. Microbiol. , vol.156 , pp. 119-128
    • Bokranz, M.1    Gutmann, M.2    Kortner, C.3    Kojro, E.4    Fahrenholz, F.5    Lauterbach, F.6    Kroger, A.7
  • 25
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • R.K. Thauer, K. Jungermann, K. Decker, Energy conservation in chemotrophic anaerobic bacteria, Bacteriol. Rev. 41 (1977) 100-180.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 26
    • 0000988148 scopus 로고
    • Metabolism of chemotrophic anaerobes: Old views and new aspects
    • D.P. Kelly, N.G. Carr (Eds.), Cambridge University Press, Cambridge
    • R.K. Thauer, J.G. Morris, Metabolism of chemotrophic anaerobes: old views and new aspects, in: D.P. Kelly, N.G. Carr (Eds.), The Microbe 1984. Part II: Prokaryotes and Eukaryotes, Cambridge University Press, Cambridge, 1984, pp. 123-168.
    • (1984) The Microbe 1984. Part II: Prokaryotes and Eukaryotes , pp. 123-168
    • Thauer, R.K.1    Morris, J.G.2
  • 28
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • J. Simon, R. Gross, M. Ringel, E. Schmidt, A. Kroger, Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon, Eur. J. Biochem. 251 (1998) 418-426.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 418-426
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, E.4    Kroger, A.5
  • 29
    • 0025847633 scopus 로고
    • Wolinella recta, Wolinella curva, Bacteroides ureolyticus, and Bacteroides gracilis are microaerophiles, not anaerobes
    • Y.-H. Han, R.M. Smibert, N.R. Krieg, Wolinella recta, Wolinella curva, Bacteroides ureolyticus, and Bacteroides gracilis are microaerophiles, not anaerobes, Int. J. Syst. Bacteriol. 41 (1991) 218-222.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , pp. 218-222
    • Han, Y.-H.1    Smibert, R.M.2    Krieg, N.R.3
  • 30
    • 0002496082 scopus 로고
    • Pathways for anaerobic electron transport
    • F.C. Neidhard, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.), ASM Press, Washington, DC
    • E.E.C. Lin, D.R. Kuritzkes, Pathways for anaerobic electron transport, in: F.C. Neidhard, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.), Eschericia coli and Salmonella - Cellular and Molecular Biology, 1, ASM Press, Washington, DC, 1987, pp. 201-221.
    • (1987) Eschericia Coli and Salmonella - Cellular and Molecular Biology , vol.1 , pp. 201-221
    • Lin, E.E.C.1    Kuritzkes, D.R.2
  • 31
    • 0027331968 scopus 로고
    • Fumarate catabolism in Helicobacter pylori
    • G.L. Mendz, S.L. Hazell, Fumarate catabolism in Helicobacter pylori, Biochem. Mol. Biol. Int. 31 (1993) 325-332.
    • (1993) Biochem. Mol. Biol. Int. , vol.31 , pp. 325-332
    • Mendz, G.L.1    Hazell, S.L.2
  • 32
    • 0027289424 scopus 로고
    • Acetyl-CoA cleavage pathway in a synthrophic propionate oxidizing bacterium growing on fumarate in the absence of methanogens
    • C.M. Plugge, C. Dijkema, A.J.M. Stams, Acetyl-CoA cleavage pathway in a synthrophic propionate oxidizing bacterium growing on fumarate in the absence of methanogens, FEMS Microbiol. Lett. 110 (1993) 71-76.
    • (1993) FEMS Microbiol. Lett. , vol.110 , pp. 71-76
    • Plugge, C.M.1    Dijkema, C.2    Stams, A.J.M.3
  • 33
    • 0022472585 scopus 로고
    • Acetate oxidation to CO2 in anaerobic bacteria via a novel pathway not involving reactions of the citric acid cycle
    • R. Schauder, B. Eikmanns, R.K. Thauer, F. Widdel, G. Fuchs, Acetate oxidation to CO2 in anaerobic bacteria via a novel pathway not involving reactions of the citric acid cycle, Arch. Microbiol. 145 (1986) 162-172.
    • (1986) Arch. Microbiol. , vol.145 , pp. 162-172
    • Schauder, R.1    Eikmanns, B.2    Thauer, R.K.3    Widdel, F.4    Fuchs, G.5
  • 34
    • 0038241205 scopus 로고
    • Anaerobic acetate oxidation to CO2 by Desulfotomaculum acetoxidans
    • A.M. Spormann, R.K. Thauer, Anaerobic acetate oxidation to CO2 by Desulfotomaculum acetoxidans, Arch. Microbiol. 150 (1988) 374-380.
    • (1988) Arch. Microbiol. , vol.150 , pp. 374-380
    • Spormann, A.M.1    Thauer, R.K.2
  • 35
    • 0031981523 scopus 로고    scopus 로고
    • Investigation of the fumarate metabolism of the synthrophic propionate-oxidizing bacterium strain MPOB
    • B.L.M. Van Kuijk, E. Schlösser, A.J.M. Stams, Investigation of the fumarate metabolism of the synthrophic propionate-oxidizing bacterium strain MPOB, Arch. Microbiol. 169 (1998) 346-352.
    • (1998) Arch. Microbiol. , vol.169 , pp. 346-352
    • Van Kuijk, B.L.M.1    Schlösser, E.2    Stams, A.J.M.3
  • 37
    • 0017567929 scopus 로고
    • The effect of different oxygen tensions on growth and enzyme activities on Campylobacter sputorum subspecies bubulus
    • H.G.D. Niekus, W. de Vries, A.H. Stouthamer, The effect of different oxygen tensions on growth and enzyme activities on Campylobacter sputorum subspecies bubulus, J. Gen. Microbiol. 103 (1977) 215-222.
    • (1977) J. Gen. Microbiol. , vol.103 , pp. 215-222
    • Niekus, H.G.D.1    De Vries, W.2    Stouthamer, A.H.3
  • 38
  • 39
    • 0020029133 scopus 로고
    • Respiratory physiology and energy conservation efficiency of Campylobacter jejuni
    • P.S. Hoofman, T.G. Goodman, Respiratory physiology and energy conservation efficiency of Campylobacter jejuni, J. Bacteriol. 150 (1982) 319-326.
    • (1982) J. Bacteriol. , vol.150 , pp. 319-326
    • Hoofman, P.S.1    Goodman, T.G.2
  • 40
    • 0026534302 scopus 로고
    • Cytochrome composition and oxygen dependent respiration-driven proton translocation in Wolinella curva, Wolinella recta, Bacteroides ureolyticus and Bacteroides gracilis
    • Y.-H. Han, R.M. Smibert, N.R. Krieg, Cytochrome composition and oxygen dependent respiration-driven proton translocation in Wolinella curva, Wolinella recta, Bacteroides ureolyticus and Bacteroides gracilis, Can. J. Microbiol. 38 (1992) 104-110.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 104-110
    • Han, Y.-H.1    Smibert, R.M.2    Krieg, N.R.3
  • 41
    • 0019165056 scopus 로고
    • Respiratory system and cytochromes in Campylobacter fetus subsp. intestinalis
    • S. Harvey, J. Lascelles, Respiratory system and cytochromes in Campylobacter fetus subsp. intestinalis, J. Bacteriol. 144 (1980) 917-922.
    • (1980) J. Bacteriol. , vol.144 , pp. 917-922
    • Harvey, S.1    Lascelles, J.2
  • 43
    • 0028898078 scopus 로고
    • Pyruvate:ferredoxin oxidoreductase in Campylobacter species
    • J.A. Daucher, N.R. Krieg, Pyruvate:ferredoxin oxidoreductase in Campylobacter species, Can. J. Microbiol. 41 (1995) 198-201.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 198-201
    • Daucher, J.A.1    Krieg, N.R.2
  • 44
    • 0029046363 scopus 로고
    • Identification of carboxylation enzymes and characteriz-ation of a novel four-subunit pyruvate: Flavodoxin oxidoreductase from Helicobacter pylori
    • N.J. Hughes, P.A. Chalk, C.L. Clayton, D.J. Kelly, Identification of carboxylation enzymes and characteriz-ation of a novel four-subunit pyruvate: flavodoxin oxidoreductase from Helicobacter pylori, J. Bacteriol. 177 (1995) 3953-3959.
    • (1995) J. Bacteriol. , vol.177 , pp. 3953-3959
    • Hughes, N.J.1    Chalk, P.A.2    Clayton, C.L.3    Kelly, D.J.4
  • 45
    • 0031083353 scopus 로고    scopus 로고
    • How Helicobacter pylori works: An overview of the metabolism of Helicobacter pylori
    • S.L. Hazell, G.L. Mendz, How Helicobacter pylori works: an overview of the metabolism of Helicobacter pylori, Helicobacter 2 (1997) 1-12.
    • (1997) Helicobacter , vol.2 , pp. 1-12
    • Hazell, S.L.1    Mendz, G.L.2
  • 48
    • 0032549098 scopus 로고    scopus 로고
    • Containment of antibiotic resitance
    • R.J. Williams, D.L. Heymann, Containment of antibiotic resitance, Science 279 (1998) 1153-1154.
    • (1998) Science , vol.279 , pp. 1153-1154
    • Williams, R.J.1    Heymann, D.L.2
  • 49
    • 0014945703 scopus 로고
    • Mode of action of the anthelmintic thiabendazole in Haemonchus cantor tus
    • R.K. Prichard, Mode of action of the anthelmintic thiabendazole in Haemonchus cantor tus, Nature 228 (1970) 684-685.
    • (1970) Nature , vol.228 , pp. 684-685
    • Prichard, R.K.1
  • 50
    • 0022355545 scopus 로고
    • A comparative study of the succinate dehydrogenase-fumarate reductase complex in the genus Trichinella
    • F. Rodriguez Caaberiro, A. Criado Fornelio, A. Jiminez Gonzalez, A comparative study of the succinate dehydrogenase-fumarate reductase complex in the genus Trichinella, Parasitology 91 (1985) 577-583.
    • (1985) Parasitology , vol.91 , pp. 577-583
    • Rodriguez Caaberiro, F.1    Criado Fornelio, A.2    Jiminez Gonzalez, A.3
  • 52
    • 0015622728 scopus 로고
    • The fumarate reductase reaction of Haemonchus contortus and the mode of action of some anthelmintics
    • R.K. Prichard, The fumarate reductase reaction of Haemonchus contortus and the mode of action of some anthelmintics, Int. J. Parasitol. 3 (1973) 409-417.
    • (1973) Int. J. Parasitol. , vol.3 , pp. 409-417
    • Prichard, R.K.1
  • 53
    • 0016701278 scopus 로고
    • Effect of cambendazole, thiabendazole, and levamisole on fumarate reductase in cambendazole-resistant and -sensitive strains of Haemonchus contortus
    • R.D. Romanowski, M.L. Rhoads, M.L. Colglazier, K.C. Kates, Effect of cambendazole, thiabendazole, and levamisole on fumarate reductase in cambendazole-resistant and -sensitive strains of Haemonchus contortus, , J. Parasitol. 61 (1975) 777-778.
    • (1975) J. Parasitol. , vol.61 , pp. 777-778
    • Romanowski, R.D.1    Rhoads, M.L.2    Colglazier, M.L.3    Kates, K.C.4
  • 54
    • 0029113366 scopus 로고
    • Fumarate reductase: A target for therapeutic Intravention against Helicobacter pylori
    • G.L. Mendz, S.L. Hazell, S. Srinivasan, Fumarate reductase: a target for therapeutic Intravention against Helicobacter pylori, Arch. Biochem. Biophys. 321 (1995) 153-159.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 153-159
    • Mendz, G.L.1    Hazell, S.L.2    Srinivasan, S.3


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